Evidence map›Paper›PMID 32188728›Full record

ArticleJournal of virology2020

Structure-Guided Mutagenesis Alters Deubiquitinating Activity and Attenuates Pathogenesis of a Murine Coronavirus.

Xufang Deng, Yafang Chen, Anna M Mielech, Matthew Hackbart, Kristina R Kesely, Robert C Mettelman, Amornrat O'Brien, Mackenzie E Chapman, Andrew D Mesecar, Susan C Baker

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 27 citations in OpenAlex.

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  9. P53 in the impaired lungs.DNA repair · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Xufang DengDepartment of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA.
Yafang ChenDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.
Anna M MielechDepartment of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA.
Matthew HackbartDepartment of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA.
Kristina R KeselyDepartment of Biochemistry, Purdue University, West Lafayette, Indiana, USA.
Robert C MettelmanDepartment of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA.
Amornrat O'BrienDepartment of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA.
Mackenzie E ChapmanDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.
Andrew D MesecarDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.
Susan C BakerDepartment of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois, USA sbaker1@luc.edu.ORCID 0000-0001-6485-8143
Loyola University Chicago · USPurdue University West Lafayette · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
Mechanisms of viral proteases in coronavirus replication and pathogenesisR01AI085089 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI BAKER, SUSAN C., MESECAR, ANDREW D · 2010 to 2019
$6.8M
Experimental Immunology Training GrantT32AI007508 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI KNIGHT, KATHERINE L. · 1997 to 2022
$4.0M
Purdue University Molecular Biophysics Training ProgramT32GM132024 · NIGMS · PURDUE UNIVERSITY · PI Angeline Marie Lyon, John Tesmer · 2019 to 2026
$2.0M
NCI NIH HHS P30 CA023168NIAID NIH HHS R01 AI085089NIAID NIH HHS T32 AI007508NIGMS NIH HHS T32 GM132024
6 · The paper itself

Abstract

Coronaviruses express a multifunctional papain-like protease, termed papain-like protease 2 (PLP2). PLP2 acts as a protease that cleaves the viral replicase polyprotein and as a deubiquitinating (DUB) enzyme which removes ubiquitin (Ub) moieties from ubiquitin-conjugated proteins. Previous

Indexed as

Amino Acid SequenceAnimalsCoronavirus InfectionsHost-Pathogen InteractionsInterferon Type IMacrophagesMiceModels, MolecularMurine hepatitis virusMutagenesisProtein ConformationStructure-Activity RelationshipUbiquitinationViral ProteinsVirulenceVirus ReplicationInterferon Type IViral ProteinscoronavirusDUB activityIFN antagonistpapain-like proteasePLP2PLP2 structure

Identifiers

PMID32188728
PMCPMC7269429
OpenAlexW3010674433

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.